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| | ==Solution Structure of the Tandem WW Domains of FBP21== | | ==Solution Structure of the Tandem WW Domains of FBP21== |
| - | <StructureSection load='2jxw' size='340' side='right'caption='[[2jxw]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2jxw' size='340' side='right'caption='[[2jxw]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2jxw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JXW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JXW FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2jxw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JXW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JXW FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">WBP4, FBP21, FNBP21 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2jxw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jxw OCA], [https://pdbe.org/2jxw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jxw RCSB], [https://www.ebi.ac.uk/pdbsum/2jxw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jxw ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2jxw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jxw OCA], [https://pdbe.org/2jxw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jxw RCSB], [https://www.ebi.ac.uk/pdbsum/2jxw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jxw ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/WBP4_HUMAN WBP4_HUMAN]] Promotes pre-mRNA splicing. A spliceosome-associated protein; may play a role in cross-intron bridging of U1 and U2 snRNPs in the mammalian A complex.<ref>PMID:9724750</ref> <ref>PMID:19592703</ref>
| + | [https://www.uniprot.org/uniprot/WBP4_HUMAN WBP4_HUMAN] Promotes pre-mRNA splicing. A spliceosome-associated protein; may play a role in cross-intron bridging of U1 and U2 snRNPs in the mammalian A complex.<ref>PMID:9724750</ref> <ref>PMID:19592703</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Huang, X]] | + | [[Category: Huang X]] |
| - | [[Category: Shi, Y]] | + | [[Category: Shi Y]] |
| - | [[Category: Wu, J]] | + | [[Category: Wu J]] |
| - | [[Category: Zhang, J]] | + | [[Category: Zhang J]] |
| - | [[Category: Fbp21]]
| + | |
| - | [[Category: Formin binding protein]]
| + | |
| - | [[Category: Metal-binding]]
| + | |
| - | [[Category: Mrna processing]]
| + | |
| - | [[Category: Mrna splicing]]
| + | |
| - | [[Category: Nucleus]]
| + | |
| - | [[Category: Polymorphism]]
| + | |
| - | [[Category: Spliceosome]]
| + | |
| - | [[Category: Wbp4]]
| + | |
| - | [[Category: Ww domain]]
| + | |
| - | [[Category: Ww domain containing protein]]
| + | |
| - | [[Category: Zinc]]
| + | |
| - | [[Category: Zinc-finger]]
| + | |
| Structural highlights
Function
WBP4_HUMAN Promotes pre-mRNA splicing. A spliceosome-associated protein; may play a role in cross-intron bridging of U1 and U2 snRNPs in the mammalian A complex.[1] [2]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Human FBP21 (formin-binding protein 21) contains a matrin-type zinc finger and two tandem WW domains. It is a component of the spliceosomes and interacts with several established splicing factors. Here we demonstrate for the first time that FBP21 is an activator of pre-mRNA splicing in vivo and that its splicing activation function and interaction with the splicing factor SIPP1 (splicing factor that interacts with PQBP1 and PP1) are both mediated by the two tandem WW domains of group III. We determined the solution structure of the tandem WW domains of FBP21 and found that the WW domains recognize peptide ligands containing either group II (PPLP) or group III (PPR) motifs. The binding interfaces involve both the XP and XP2 grooves of the two WW domains. Significantly, the tandem WW domains of FBP21 are connected by a highly flexible region, enabling their simultaneous interaction with two proline-rich motifs of SIPP1. The strong interaction between SIPP1 and FBP21 can be explained by the conjugation of two low affinity interactions with the tandem WW domains. Our study provides a structural basis for understanding the molecular mechanism underlying the functional implication of FBP21 and the biological specificity of tandem WW domains.
Structure and function of the two tandem WW domains of the pre-mRNA splicing factor FBP21 (formin-binding protein 21).,Huang X, Beullens M, Zhang J, Zhou Y, Nicolaescu E, Lesage B, Hu Q, Wu J, Bollen M, Shi Y J Biol Chem. 2009 Sep 11;284(37):25375-87. Epub 2009 Jul 10. PMID:19592703[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Bedford MT, Reed R, Leder P. WW domain-mediated interactions reveal a spliceosome-associated protein that binds a third class of proline-rich motif: the proline glycine and methionine-rich motif. Proc Natl Acad Sci U S A. 1998 Sep 1;95(18):10602-7. PMID:9724750
- ↑ Huang X, Beullens M, Zhang J, Zhou Y, Nicolaescu E, Lesage B, Hu Q, Wu J, Bollen M, Shi Y. Structure and function of the two tandem WW domains of the pre-mRNA splicing factor FBP21 (formin-binding protein 21). J Biol Chem. 2009 Sep 11;284(37):25375-87. Epub 2009 Jul 10. PMID:19592703 doi:10.1074/jbc.M109.024828
- ↑ Huang X, Beullens M, Zhang J, Zhou Y, Nicolaescu E, Lesage B, Hu Q, Wu J, Bollen M, Shi Y. Structure and function of the two tandem WW domains of the pre-mRNA splicing factor FBP21 (formin-binding protein 21). J Biol Chem. 2009 Sep 11;284(37):25375-87. Epub 2009 Jul 10. PMID:19592703 doi:10.1074/jbc.M109.024828
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